Abstract
A strategy has been developed for caging proteins that are endogenously regulated by phosphorylation. A key phosphorylatable serine in cofilin, an F-actin cleaving protein, was replaced with a nonphosphorylatable cysteine. The latter conversion ensures that the protein is no longer regulated by endogenous protein kinases. The cysteine residue was subsequently covalently modified with a negatively charged caging moiety, which electrostatically mimics the natural serine phosphate present in the inactive wild-type protein. Photoremoval of the cage generates an active protein, which cannot be switched off by endogenous protein kinases. Caged cofilin, and its irradiated counterpart, display the anticipated F-actin depolymerization and severing activities.
Original language | English (US) |
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Pages (from-to) | 2440-2441 |
Number of pages | 2 |
Journal | Journal of the American Chemical Society |
Volume | 124 |
Issue number | 11 |
DOIs | |
State | Published - Mar 20 2002 |
ASJC Scopus subject areas
- Catalysis
- General Chemistry
- Biochemistry
- Colloid and Surface Chemistry